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Database: UniProt
Entry: A0A0H0XR54_9SPHN
LinkDB: A0A0H0XR54_9SPHN
Original site: A0A0H0XR54_9SPHN 
ID   A0A0H0XR54_9SPHN        Unreviewed;       506 AA.
AC   A0A0H0XR54;
DT   16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT   16-SEP-2015, sequence version 1.
DT   24-JAN-2024, entry version 32.
DE   RecName: Full=Replicative DNA helicase {ECO:0000256|ARBA:ARBA00021957, ECO:0000256|RuleBase:RU362085};
DE            EC=3.6.4.12 {ECO:0000256|ARBA:ARBA00012551, ECO:0000256|RuleBase:RU362085};
GN   ORFNames=AAV99_02485 {ECO:0000313|EMBL:KLI64481.1};
OS   Aurantiacibacter marinus.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC   Erythrobacteraceae; Aurantiacibacter.
OX   NCBI_TaxID=874156 {ECO:0000313|EMBL:KLI64481.1, ECO:0000313|Proteomes:UP000053455};
RN   [1] {ECO:0000313|EMBL:KLI64481.1, ECO:0000313|Proteomes:UP000053455}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HWDM-33 {ECO:0000313|EMBL:KLI64481.1,
RC   ECO:0000313|Proteomes:UP000053455};
RA   Zhuang L., Liu Y., Shao Z.;
RT   "The draft genome sequence of Erythrobacter marinus HWDM-33.";
RL   Submitted (APR-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Participates in initiation and elongation during chromosome
CC       replication; it exhibits DNA-dependent ATPase activity and contains
CC       distinct active sites for ATP binding, DNA binding, and interaction
CC       with DnaC protein, primase, and other prepriming proteins.
CC       {ECO:0000256|ARBA:ARBA00003574, ECO:0000256|RuleBase:RU362085}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.12;
CC         Evidence={ECO:0000256|ARBA:ARBA00001665,
CC         ECO:0000256|RuleBase:RU362085};
CC   -!- SIMILARITY: Belongs to the helicase family. DnaB subfamily.
CC       {ECO:0000256|ARBA:ARBA00008428, ECO:0000256|RuleBase:RU362085}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KLI64481.1}.
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DR   EMBL; LBHU01000001; KLI64481.1; -; Genomic_DNA.
DR   RefSeq; WP_047092345.1; NZ_LDCP01000001.1.
DR   AlphaFoldDB; A0A0H0XR54; -.
DR   STRING; 874156.GCA_001021555_00783; -.
DR   PATRIC; fig|874156.12.peg.517; -.
DR   OrthoDB; 9773982at2; -.
DR   Proteomes; UP000053455; Unassembled WGS sequence.
DR   GO; GO:1990077; C:primosome complex; IEA:UniProtKB-UniRule.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0003678; F:DNA helicase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006269; P:DNA replication, synthesis of RNA primer; IEA:UniProtKB-UniRule.
DR   CDD; cd00984; DnaB_C; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   InterPro; IPR003593; AAA+_ATPase.
DR   InterPro; IPR036185; DNA_heli_DnaB-like_N_sf.
DR   InterPro; IPR007692; DNA_helicase_DnaB.
DR   InterPro; IPR007694; DNA_helicase_DnaB-like_C.
DR   InterPro; IPR007693; DNA_helicase_DnaB-like_N.
DR   InterPro; IPR016136; DNA_helicase_N/primase_C.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   NCBIfam; TIGR00665; DnaB; 1.
DR   PANTHER; PTHR30153:SF2; REPLICATIVE DNA HELICASE; 1.
DR   PANTHER; PTHR30153; REPLICATIVE DNA HELICASE DNAB; 1.
DR   Pfam; PF00772; DnaB; 1.
DR   Pfam; PF03796; DnaB_C; 1.
DR   SMART; SM00382; AAA; 1.
DR   SUPFAM; SSF48024; N-terminal domain of DnaB helicase; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   PROSITE; PS51199; SF4_HELICASE; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU362085};
KW   DNA replication {ECO:0000256|ARBA:ARBA00022705,
KW   ECO:0000256|RuleBase:RU362085};
KW   DNA-binding {ECO:0000256|ARBA:ARBA00023125, ECO:0000256|RuleBase:RU362085};
KW   Helicase {ECO:0000256|ARBA:ARBA00022806, ECO:0000256|RuleBase:RU362085};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU362085};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|RuleBase:RU362085};
KW   Primosome {ECO:0000256|ARBA:ARBA00022515, ECO:0000256|RuleBase:RU362085};
KW   Reference proteome {ECO:0000313|Proteomes:UP000053455}.
FT   DOMAIN          196..499
FT                   /note="SF4 helicase"
FT                   /evidence="ECO:0000259|PROSITE:PS51199"
FT   REGION          1..20
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   506 AA;  56134 MW;  B8DBDE9C17201F32 CRC64;
     MSDEALLTRS DSKSADGAPA GKALPTNLEA EAAFIGAVLI DNRVLEELPI ELMPKHFYAP
     VHQRIYDRIL ISVEKQMIVT PVTLKPYFEN DEGLKELGGS AYLAQLTADG QGLLAPRELA
     QQIYDLALLR ELVGVGRELV ENALDTSQDV EPMRQIESAE ARLFEVAEGA VSENTGTSFR
     SASHEAIRMV EAAMNSGGGL SGKTTGLELI DNKTAGLHNS DLIILAGRPG MGKSSLAMNI
     AFNCAEEHMR FQRDGGPHNY GAPAAFFSLE MSADQLATRI LAEQAEVSSE ALRSGKLNRE
     EFQKLSYAAQ KLSELQLFID DTPALTISGL RTRARRLKRR HDIGLIVVDY LQLLQGSGRA
     SDNRVNEISE ISRGLKTLAK ELQVPVIALS QLSRAVESRE DKRPMLSDLR ESGSIEQDAD
     MVWFIFRAEY YHEASRPDMP NETSSESDQE KYRVWEDRYL ELKNKATLMV AKQRHGSTGN
     VPLHFQSEFT KFTSPNMKDY SDYGFE
//
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